메뉴 건너뛰기




Volumn 115, Issue 24, 2002, Pages 5003-5012

Indentification of CfNek, a novel member of the NIMA family of cell cycle regulators, as a polypeptide copurifying with tubulin polyglutamylation activity in Crithidia

Author keywords

Cell cycle; Crithidia; NIMA kinases; Polyglutamylation; Post translational modification; Tubulin

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINO ACID; BETA CASEIN; CELL CYCLE PROTEIN; COMPLEMENTARY DNA; GLYCINE; HYDROXYAPATITE; MICROTUBULE ASSOCIATED PROTEIN; NICKEL; PLECKSTRIN; POLYPEPTIDE; PROTEIN CFNEK; PROTEIN KINASE; RECOMBINANT ENZYME; REGULATOR PROTEIN; TUBULIN; UNCLASSIFIED DRUG; NEK1 PROTEIN KINASE; POLYGLUTAMIC ACID; PRIMER DNA; PROTEIN SERINE THREONINE KINASE; PROTEIN TYROSINE KINASE; RECOMBINANT PROTEIN;

EID: 0037115726     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00170     Document Type: Article
Times cited : (14)

References (47)
  • 1
    • 0018841905 scopus 로고
    • Tubulinyl-tyrosine-carboxy-peptidase from chicken brain: Properties and partial purification
    • Argarana, C. E., Barra, H. S. and Caputto, R. (1980). Tubulinyl-tyrosine-carboxy-peptidase from chicken brain: properties and partial purification. J. Neurochem. 34, 114-118.
    • (1980) J. Neurochem. , vol.34 , pp. 114-118
    • Argarana, C.E.1    Barra, H.S.2    Caputto, R.3
  • 3
    • 0032517865 scopus 로고    scopus 로고
    • Centriole Dissassembly in vivo and its effect on centrosome structure and function in vertebrate cells
    • Bobinnec, Y., Khodjakov, A., Mir, L. M., Rieder, C. L., Eddé, B. and Bornens, M. (1998b). Centriole Dissassembly in vivo and its effect on centrosome structure and function in vertebrate cells. J. Cell Biol. 143, 1575-1589.
    • (1998) J. Cell Biol. , vol.143 , pp. 1575-1589
    • Bobinnec, Y.1    Khodjakov, A.2    Mir, L.M.3    Rieder, C.L.4    Eddé, B.5    Bornens, M.6
  • 4
    • 0035918287 scopus 로고    scopus 로고
    • Differential binding regulation of microtubule associated proteins MAP1A, MAP1B, and MAP2 by tubulin polyglutamylation
    • Bonnet, C., Boucher, D., Lazereg, S., Pedrotti, B., Islam, K., Denoulet, P. and Larcher, J.-C. (2001). Differential binding regulation of microtubule associated proteins MAP1A, MAP1B, and MAP2 by tubulin polyglutamylation. J. Biol. Chem 276, 12839-12848.
    • (2001) J. Biol. Chem , vol.276 , pp. 12839-12848
    • Bonnet, C.1    Boucher, D.2    Lazereg, S.3    Pedrotti, B.4    Islam, K.5    Denoulet, P.6    Larcher, J.-C.7
  • 5
    • 0028110393 scopus 로고
    • Polyglutamylation of tubulin as a progressive regulator of in vitro interactions between the microtubule-associated protein tau and tubulin
    • Boucher, D., Larcher, J.-C., Gros, F. and Denoulet, P. (1994). Polyglutamylation of tubulin as a progressive regulator of in vitro interactions between the microtubule-associated protein tau and tubulin. Biochemistry 33, 12471-12477.
    • (1994) Biochemistry , vol.33 , pp. 12471-12477
    • Boucher, D.1    Larcher, J.-C.2    Gros, F.3    Denoulet, P.4
  • 6
    • 0034604329 scopus 로고    scopus 로고
    • Mitotic histone H3 phosphorylation by the NIMA kinase in Aspergillus nidulans
    • De Souza, C. P. C., Osmani, A. H., Wu, L.-P., Spotts, J. L. and Osmani, S. A. (2000). Mitotic histone H3 phosphorylation by the NIMA kinase in Aspergillus nidulans. Cell 102, 293-302.
    • (2000) Cell , vol.102 , pp. 293-302
    • De Souza, C.P.C.1    Osmani, A.H.2    Wu, L.-P.3    Spotts, J.L.4    Osmani, S.A.5
  • 7
    • 0032004968 scopus 로고    scopus 로고
    • Tubulin tyrosine ligase: A shared fold with the glutathione synthetase ADP-forming family
    • Dideberg, O. and Bertrand, J. (1998). Tubulin tyrosine ligase: a shared fold with the glutathione synthetase ADP-forming family. Trends Biochem. Sci. 23, 57-58.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 57-58
    • Dideberg, O.1    Bertrand, J.2
  • 9
    • 0015385595 scopus 로고
    • Rat brain microtubule protein: Purification and determination of covalently bound phosphate and carbohydrate
    • Eipper, B. A. (1972). Rat brain microtubule protein: purification and determination of covalently bound phosphate and carbohydrate. Proc. Natl. Acad. Sci. USA 69, 2283-2287.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 2283-2287
    • Eipper, B.A.1
  • 11
    • 0032518798 scopus 로고    scopus 로고
    • A centrosomal function for the human Nek2 kinase, a member of the NIMA family of cell cycle regulators
    • Fry, A. M., Meraldi, P. and Nigg, E. A. (1998). A centrosomal function for the human Nek2 kinase, a member of the NIMA family of cell cycle regulators. EMBO J. 17, 470-481.
    • (1998) EMBO J. , vol.17 , pp. 470-481
    • Fry, A.M.1    Meraldi, P.2    Nigg, E.A.3
  • 12
    • 0034091353 scopus 로고    scopus 로고
    • The NIMA related kinase X-Nek2B is required for efficient assemlby of the zygotic centrosome in Xenopus laevis
    • Fry, A. M., Descombes, P., Twomey, C., Bacchieri, R. and Nigg, E. A. (2000). The NIMA related kinase X-Nek2B is required for efficient assemlby of the zygotic centrosome in Xenopus laevis. J. Cell. Sci. 113, 1973-1984.
    • (2000) J. Cell. Sci. , vol.113 , pp. 1973-1984
    • Fry, A.M.1    Descombes, P.2    Twomey, C.3    Bacchieri, R.4    Nigg, E.A.5
  • 14
    • 0027276149 scopus 로고
    • A Trypanosoma brucei gene family encoding protein kinases with catalytic domains structurally related to Nek1 and NIMA
    • Gale, M., Jr and Parsons, M. (1993). A Trypanosoma brucei gene family encoding protein kinases with catalytic domains structurally related to Nek1 and NIMA. Mol. Biochem. Parasitol. 59, 111-121.
    • (1993) Mol. Biochem. Parasitol. , vol.59 , pp. 111-121
    • Gale M., Jr.1    Parsons, M.2
  • 16
    • 0036558294 scopus 로고    scopus 로고
    • DdNek2, the first non-vertebrate homologue of human Nek2 is involved in the formation of microtubule-organizing centers
    • Gräf, R. (2002). DdNek2, the first non-vertebrate homologue of human Nek2 is involved in the formation of microtubule-organizing centers. J. Cell Sci. 115, 1919-1929.
    • (2002) J. Cell Sci. , vol.115 , pp. 1919-1929
    • Gräf, R.1
  • 17
    • 0029020282 scopus 로고
    • The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S. K. and Hunter, T. (1995). The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9, 576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 19
    • 0021993649 scopus 로고
    • Chlamydomonas α-tubulin is post-translationally mocdified by acetylation of the ε-aminogroup of a lysine
    • L'Hernault, S. W. and Rosenbaum, J. L. (1985). Chlamydomonas α-tubulin is post-translationally mocdified by acetylation of the ε-aminogroup of a lysine. Biochemistry 24, 473-478.
    • (1985) Biochemistry , vol.24 , pp. 473-478
    • L'Hernault, S.W.1    Rosenbaum, J.L.2
  • 20
    • 0029028584 scopus 로고
    • Evidence for a NIMA-like mitotic pathway in vertebrate cells
    • Lu, K. P. and Hunter, T. (1995). Evidence for a NIMA-like mitotic pathway in vertebrate cells. Cell 81, 413-424.
    • (1995) Cell , vol.81 , pp. 413-424
    • Lu, K.P.1    Hunter, T.2
  • 21
    • 0027512931 scopus 로고
    • Properties and regulation of the cell-cycle specific NIMA protein kinase of Aspergillus nidulans
    • Lu, K. P., Osmani, S. A. and Means, A. R. (1993). Properties and regulation of the cell-cycle specific NIMA protein kinase of Aspergillus nidulans. J. Biol. Chem. 268, 8769-8776.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8769-8776
    • Lu, K.P.1    Osmani, S.A.2    Means, A.R.3
  • 22
    • 0031039519 scopus 로고    scopus 로고
    • Tubulin post-translational modifications. Enzymes and their mechanisms of action
    • MacRae, T. H. (1997). Tubulin post-translational modifications. Enzymes and their mechanisms of action. Eur. J. Biochem. 244, 265-278.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 265-278
    • MacRae, T.H.1
  • 23
    • 0023649631 scopus 로고
    • The monogenetic protozoan Crithidia fasciculata contains a transcriptionally active, multi-copy mini-exon sequence
    • Muhich, M. L., Hughes, D. F., Simpson, A. M. and Simpson, L. (1987). The monogenetic protozoan Crithidia fasciculata contains a transcriptionally active, multi-copy mini-exon sequence. Nucleic Acid. Res. 15, 3141-3153.
    • (1987) Nucleic Acid. Res. , vol.15 , pp. 3141-3153
    • Muhich, M.L.1    Hughes, D.F.2    Simpson, A.M.3    Simpson, L.4
  • 24
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αβ tubulin dimer by electron crystallography
    • Nogales, E., Wolf, S. G. and Downing, K. H. (1998). Structure of the αβ tubulin dimer by electron crystallography. Nature 391, 199-202.
    • (1998) Nature , vol.391 , pp. 199-202
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 26
    • 0034681137 scopus 로고    scopus 로고
    • Mechanism of single-headed processivity: Diffusional anhoring between the K-loop of kinesin and the C terminus of tubulin
    • Okada, Y. and Hirokawa, N. (2000). Mechanism of single-headed processivity: Diffusional anhoring between the K-loop of kinesin and the C terminus of tubulin. Proc. Natl. Acad. Sci. USA 97, 640-645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 640-645
    • Okada, Y.1    Hirokawa, N.2
  • 27
    • 0024294395 scopus 로고
    • Mitotic induction and maintenance by overexpression of a G2-specific gene that encodes a potential protein kinase
    • Osmani, S. A., Pu, R. T. and Morris, N. R. (1988). Mitotic induction and maintenance by overexpression of a G2-specific gene that encodes a potential protein kinase. Cell 53, 237-244.
    • (1988) Cell , vol.53 , pp. 237-244
    • Osmani, S.A.1    Pu, R.T.2    Morris, N.R.3
  • 28
    • 0025861473 scopus 로고
    • Activation of the nimA protein kinase plays a unique role during mitosis that cannot be bypassed by absence of the bimE checkpoint
    • Osmani, A. H., O'Donell, K., Pu, R. T. and Osamani, S. A. (1991). Activation of the nimA protein kinase plays a unique role during mitosis that cannot be bypassed by absence of the bimE checkpoint. EMBO. J. 10, 2669-2679.
    • (1991) EMBO. J. , vol.10 , pp. 2669-2679
    • Osmani, A.H.1    O'Donell, K.2    Pu, R.T.3    Osamani, S.A.4
  • 29
    • 0024583552 scopus 로고
    • Complete separation of tyrosinated, detyrosinated and nontyrosinable brain tubulin subpopulations using affinity chromatography
    • Paturle, L., Wehland, J., Margolis, R. L. and Job, D. (1989). Complete separation of tyrosinated, detyrosinated and nontyrosinable brain tubulin subpopulations using affinity chromatography. Biochemistry 28, 2698-2704.
    • (1989) Biochemistry , vol.28 , pp. 2698-2704
    • Paturle, L.1    Wehland, J.2    Margolis, R.L.3    Job, D.4
  • 30
    • 0029052804 scopus 로고
    • Isolation of a functional homolog of the cell-cycle-specific NIMA protein kinase of Aspergillus nidulans and functional analysis of conserved residues
    • Pu, R. T., Xu, G., Wu, L., Vierula, J., O'Donnell, K., Ye, X. S. and Osmani, S. A. (1995). Isolation of a functional homolog of the cell-cycle-specific NIMA protein kinase of Aspergillus nidulans and functional analysis of conserved residues. J. Biol. Chem. 270, 18110-18116.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18110-18116
    • Pu, R.T.1    Xu, G.2    Wu, L.3    Vierula, J.4    O'Donnell, K.5    Ye, X.S.6    Osmani, S.A.7
  • 31
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M. and Rogers, S. W. (1996). PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21, 267-271.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 33
    • 0032499669 scopus 로고    scopus 로고
    • Tubulin polyglutamylase: Partial purification and enzymatic properties
    • Regnard, C., Audebert, S., Desbruyères, E., Denoulet, P. and Eddé, B. (1998). Tubulin polyglutamylase: partial purification and enzymatic properties. Biochemistry 37, 8395-8404.
    • (1998) Biochemistry , vol.37 , pp. 8395-8404
    • Regnard, C.1    Audebert, S.2    Desbruyères, E.3    Denoulet, P.4    Eddé, B.5
  • 34
    • 0033491708 scopus 로고    scopus 로고
    • Tubulin polyglutamyase: Isozmyic variants and regulation during the cell cycle in HeLa cells
    • Regnard, C., Desbruyères, E., Denoulet, P. and Eddé, B. (1999). Tubulin polyglutamyase: isozmyic variants and regulation during the cell cycle in HeLa cells. J. Cell Sci. 112, 4281-4289.
    • (1999) J. Cell Sci. , vol.112 , pp. 4281-4289
    • Regnard, C.1    Desbruyères, E.2    Denoulet, P.3    Eddé, B.4
  • 36
    • 0034597639 scopus 로고    scopus 로고
    • Functions for tubulin modifications at last
    • Rosenbaum, J. (2000). Functions for tubulin modifications at last. Curr. Biol. 10, R801-R803.
    • (2000) Curr. Biol. , vol.10
    • Rosenbaum, J.1
  • 37
    • 0031049174 scopus 로고    scopus 로고
    • Subpellicular and flagellar microtubules of Trypanosoma brucei are extensively glutamylated
    • Schneider, A., Plessmann, U. and Weber, K. (1997). Subpellicular and flagellar microtubules of Trypanosoma brucei are extensively glutamylated. J. Cell Sci. 110, 431-437.
    • (1997) J. Cell Sci. , vol.110 , pp. 431-437
    • Schneider, A.1    Plessmann, U.2    Weber, K.3
  • 38
    • 0034678923 scopus 로고    scopus 로고
    • Nek2B, a novel maternal form of Nek2 kinase, is essential for the assembly and maintenance of centrosomes in early Xenopus embryos
    • Uto, K. and Sagata, N. (2000). Nek2B, a novel maternal form of Nek2 kinase, is essential for the assembly and maintenance of centrosomes in early Xenopus embryos. EMBO J. 19, 1816-1826.
    • (2000) EMBO J. , vol.19 , pp. 1816-1826
    • Uto, K.1    Sagata, N.2
  • 40
    • 0036125515 scopus 로고    scopus 로고
    • Polyglycylation of β-tubulin maintains axonemal architecture and affects cytokinesis in Tetrahymena
    • Thazhath, R., Liu, C. and Gaertig, J. (2002). Polyglycylation of β-tubulin maintains axonemal architecture and affects cytokinesis in Tetrahymena. Nat. Cell Biol. 4, 256-259.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 256-259
    • Thazhath, R.1    Liu, C.2    Gaertig, J.3
  • 41
    • 0034722373 scopus 로고    scopus 로고
    • Engineering the processive run length of the kinesin motor
    • Thorn, K. S., Ubersax, J. A. and Vale, R. D. (2000). Engineering the processive run length of the kinesin motor. J. Cell Biol. 151, 1093-1100.
    • (2000) J. Cell Biol. , vol.151 , pp. 1093-1100
    • Thorn, K.S.1    Ubersax, J.A.2    Vale, R.D.3
  • 42
    • 0031463883 scopus 로고    scopus 로고
    • Post-translational modifications of α- and β-tubulin in Giardia lamblia, an ancient eukaryote
    • Weber, K., Schneider, A., Westermann, S., Müller, N. and Plessmann, U. (1997). Post-translational modifications of α- and β-tubulin in Giardia lamblia, an ancient eukaryote. FEBS Lett. 419, 87-91.
    • (1997) FEBS Lett. , vol.419 , pp. 87-91
    • Weber, K.1    Schneider, A.2    Westermann, S.3    Müller, N.4    Plessmann, U.5
  • 43
    • 0034710171 scopus 로고    scopus 로고
    • Cloning and recombinant expression of the La RNA-binding protein from Trypanosoma brucei
    • 1492
    • Westermann, S. and Weber, K. (2000). Cloning and recombinant expression of the La RNA-binding protein from Trypanosoma brucei. Biochim. Biophys. Acta 1492, 90-94.
    • (2000) Biochim. Biophys. Acta , pp. 90-94
    • Westermann, S.1    Weber, K.2
  • 44
    • 0032839187 scopus 로고    scopus 로고
    • Isolation of Crithidia tubulin polyglutamylase; binding to microtubules and tubulin, and glutamylation of mammalian brain α- and β-tubulins
    • Westermann, S., Schneider, A., Horn, E. K. and Weber, K. (1999a). Isolation of Crithidia tubulin polyglutamylase; binding to microtubules and tubulin, and glutamylation of mammalian brain α- and β-tubulins. J. Cell Sci. 112, 2185-2193.
    • (1999) J. Cell Sci. , vol.112 , pp. 2185-2193
    • Westermann, S.1    Schneider, A.2    Horn, E.K.3    Weber, K.4
  • 45
    • 0032835183 scopus 로고    scopus 로고
    • Synthetic peptides identify the minimal sequence requirements of tubulin polyglutamylase in side chain elongation
    • Westermann, S., Plessmann, U. and Weber, K. (1999b). Synthetic peptides identify the minimal sequence requirements of tubulin polyglutamylase in side chain elongation. FEBS Lett. 459, 90-94.
    • (1999) FEBS Lett. , vol.459 , pp. 90-94
    • Westermann, S.1    Plessmann, U.2    Weber, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.